ID   A0A0J6YTA4_9BACT        Unreviewed;      1059 AA.
AC   A0A0J6YTA4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KMP11791.1};
GN   ORFNames=UR09_02515 {ECO:0000313|EMBL:KMP11791.1};
OS   Candidatus Nitromaritima sp. SCGC AAA799-A02.
OC   Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC   Nitrospinales; Nitrospinaceae; Candidatus Nitromaritima.
OX   NCBI_TaxID=1628278 {ECO:0000313|EMBL:KMP11791.1, ECO:0000313|Proteomes:UP000035948};
RN   [1] {ECO:0000313|EMBL:KMP11791.1, ECO:0000313|Proteomes:UP000035948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC_AAA799_A02 {ECO:0000313|EMBL:KMP11791.1};
RA   Ngugi D.K., Blom J., Stepanauskas R., Stingl U.;
RT   "Diversification and niche adaptations of Nitrospina-like bacteria in the
RT   poly-extreme interfaces of the Atlantis II Deep brine from the Red Sea.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMP11791.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JZKI01000014; KMP11791.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6YTA4; -.
DR   PATRIC; fig|1628278.3.peg.242; -.
DR   Proteomes; UP000035948; Unassembled WGS sequence.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR   Gene3D; 1.20.120.1510; -; 2.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 2.
DR   InterPro; IPR023057; GlnE.
DR   InterPro; IPR005190; GlnE_rpt_dom.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   PANTHER; PTHR30621:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME; 1.
DR   PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 2.
DR   Pfam; PF03710; GlnE; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035948};
KW   Transferase {ECO:0000256|ARBA:ARBA00022695}.
FT   DOMAIN          102..359
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          381..527
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          642..885
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          907..1050
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   1059 AA;  122042 MW;  A9E92BF56FFE2D70 CRC64;
     MHIPTKLIES IHKRHPWEEG LATPLKELKF DDPEKAWKNL LILSTHCNFP SLFSNFFPSL
     LKELARSYNP DLALRNLERF AESILDKDYF YTILSSSPKL LEALVVLFSG SQVLTDTLLS
     DPSFFDWLKE PDTLDKSKSR DGFMRDFYDL AGTDYLSDKT PSLIRKFKKR EYIRIGLRDL
     LGKTDFRETG MDVSLLADVC LQVAYEYADR VCKKNFGAPF YEDADGNWKE AEFTIIGMGK
     LGGLELNYSS DIDIIYIYTS SKGETRLEEG SQTAVMRISN HEYFTKLALL ITRTINEITP
     EGNVFRVDLD LRPEGKSGEI VNSLASCEIY YQSWGRTWER QALMKARVSA GSEALGEEFF
     SLLEPFIYRR SLDFSAVEEI RAMKKKINQS LKRNKTGGSN IKLGYGGIRE VEFTVQAYQL
     LFGGRDKSLR IANTLEVLGK LKELGFLMEE DHDRLREAYI FLRNLENRVQ ISFGLQTHLL
     PENEDQLSVL ARKMRLDGAS HKARAEHLMR EFDRHTQFVG NLFSGLFAEN KKKEAAEIAE
     KEYRRRLSDR GELSPEVLER ISFIDPKRAL QFLETLRDGP QFSHPSEKSI QEFYALLPKI
     LEICGRVPMP NSAVENLARF VEMSRARDSF LSLFHSNEKL LELLLTLFGS SDYLSSILIK
     QPGVVDVLRN LDFIHRFRHP AKIVEELSRS LRDFGDFEAK KIFLRRFKQG EELRVGIRYL
     IREADLEGTL ADLSSLADIY LQTAYLTALE ELKQRYNKKV FLPMDFAIIG MGKLGGCELN
     FGSDLDIVFV YDEPKEDRPL SEELVPYYAK LSQLMYELTS QMTSAGYAYK VDADLRPEGA
     SGVLVMSVKG YEDYFKNRAR VWEQQAMTRA RFVAGNERVG QDFLEVARKF TYRPKLEYGS
     LIEISRLRER MEKELAREAS RGKNVKLGFG GLADIEFTVQ ILQMMHGYKH FKLRETNTLA
     VVAQFDALGI LDYEETDRLR HNYLFLRNVE CALRILNPAS SNHLPKGKDF LRVLARLLGY
     EEKNDDDPSA LFMEDYDRVT KEVRAFYRKT IDTLLRTSL
//